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Protein

Erabutoxin a

Gene
N/A
Organism
Laticauda semifasciata (Black-banded sea krait) (Pseudolaticauda semifasciata)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds with high affinity to muscular nicotinic acetylcholine receptors (nAChRs) and with low affinity to neuronal alpha-7 nAChRs and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission. Produces peripheral paralysis by blocking neuromuscular transmission at the postsynaptic site. Blocks the extracellular increase of dopamine evoked by nicotine at 4.2 µM concentrations.2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acetylcholine receptor inhibiting toxin, Ion channel impairing toxin, Neurotoxin, Postsynaptic neurotoxin, Toxin

Names & Taxonomyi

Protein namesi
Recommended name:
Erabutoxin a
Short name:
ETXA
Alternative name(s):
Short neurotoxin 1a
OrganismiLaticauda semifasciata (Black-banded sea krait) (Pseudolaticauda semifasciata)
Taxonomic identifieri8631 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaSerpentesColubroideaElapidaeLaticaudinaeLaticauda

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Toxic dosei

LD50 is 0.15 mg/kg by intramuscular injection.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationAdd
BLAST
Chaini22 – 8362Erabutoxin aPRO_0000035446Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 45
Disulfide bondi38 ↔ 62
Disulfide bondi64 ↔ 75
Disulfide bondi76 ↔ 81

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed by the venom gland.Curated

Structurei

Secondary structure

1
83
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 253Combined sources
Beta strandi35 – 373Combined sources
Beta strandi45 – 528Combined sources
Beta strandi55 – 639Combined sources
Beta strandi72 – 765Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QKDX-ray1.49A/B22-83[»]
1QKEX-ray1.50A22-83[»]
2ERAX-ray1.81A22-83[»]
3ERAX-ray1.70A/B22-83[»]
5EBXX-ray2.00A22-83[»]
ProteinModelPortaliP60775.
SMRiP60775. Positions 22-83.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60775.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG006553.

Family and domain databases

InterProiIPR003571. Snake_3FTx.
IPR018354. Snake_toxin_con_site.
[Graphical view]
PROSITEiPS00272. SNAKE_TOXIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P60775-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTLLLTLVV VTIVCLDLGY TRICFNHQSS QPQTTKTCSP GESSCYNKQW
60 70 80
SDFRGTIIER GCGCPTVKPG IKLSCCESEV CNN
Length:83
Mass (Da):9,137
Last modified:July 21, 1986 - v1
Checksum:iBBB499DA33440F44
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02533 mRNA. Translation: CAA26373.1.
AB017932 mRNA. Translation: BAA75752.1.
AB098526 Genomic DNA. Translation: BAC78199.1.
AB098527 Genomic DNA. Translation: BAC78200.1.
PIRiA01703. N1LT2E.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02533 mRNA. Translation: CAA26373.1.
AB017932 mRNA. Translation: BAA75752.1.
AB098526 Genomic DNA. Translation: BAC78199.1.
AB098527 Genomic DNA. Translation: BAC78200.1.
PIRiA01703. N1LT2E.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QKDX-ray1.49A/B22-83[»]
1QKEX-ray1.50A22-83[»]
2ERAX-ray1.81A22-83[»]
3ERAX-ray1.70A/B22-83[»]
5EBXX-ray2.00A22-83[»]
ProteinModelPortaliP60775.
SMRiP60775. Positions 22-83.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG006553.

Miscellaneous databases

EvolutionaryTraceiP60775.

Family and domain databases

InterProiIPR003571. Snake_3FTx.
IPR018354. Snake_toxin_con_site.
[Graphical view]
PROSITEiPS00272. SNAKE_TOXIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequence analysis of the cDNA encoding a snake neurotoxin precursor."
    Tamiya T., Lamouroux A., Julien J.-F., Grima B., Mallet J., Fromageot P., Menez A.
    Biochimie 67:185-189(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.
  2. "Classification of sea snakes in genus Laticauda by nucleotide sequences encoding short chain neurotoxins."
    Kariya Y., Araki S., Agu H., Tamiya T., Tsuchiya T.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Venom gland.
  3. "Molecular evolution and diversification of snake toxin genes, revealed by analysis of intron sequences."
    Fujimi T.J., Nakajyo T., Nishimura E., Ogura E., Tsuchiya T., Tamiya T.
    Gene 313:111-118(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Liver.
  4. "The amino acid sequences of erabutoxins, neurotoxic proteins of sea-snake (Laticauda semifasciata) venom."
    Sato S., Tamiya N.
    Biochem. J. 122:453-461(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-83, SUBCELLULAR LOCATION.
  5. "Correction of partial amino acid sequence of erabutoxins."
    Maeda N., Tamiya N.
    Biochem. J. 167:289-291(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  6. "The disulphide bonds of erabutoxin a, a neurotoxic protein of a sea-snake (Laticauda semifasciata) venom."
    Endo Y., Sato S., Ishii S., Tamiya N.
    Biochem. J. 122:463-467(1971) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  7. "Only snake curaremimetic toxins with a fifth disulfide bond have high affinity for the neuronal alpha7 nicotinic receptor."
    Servent D., Winckler-Dietrich V., Hu H.-Y., Kessler P., Drevet P., Bertrand D., Menez A.
    J. Biol. Chem. 272:24279-24286(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Tissue: Venom.
  8. "Effects of alpha-erabutoxin, alpha-bungarotoxin, alpha-cobratoxin and fasciculin on the nicotine-evoked release of dopamine in the rat striatum in vivo."
    Dajas-Bailador F., Costa G., Dajas F., Emmett S.
    Neurochem. Int. 33:307-312(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Three-dimensional structure of neurotoxin a from venom of the Philippines sea snake."
    Tsernoglou D., Petsko G.A.
    Proc. Natl. Acad. Sci. U.S.A. 74:971-974(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-83, DISULFIDE BONDS.
  10. "The crystal structure of erabutoxin a at 2.0-A resolution."
    Corfield P.W.R., Lee T.-J., Low B.W.
    J. Biol. Chem. 264:9239-9242(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 22-83, DISULFIDE BONDS.
  11. "Genetic engineering of snake toxins. The functional site of Erabutoxin a, as delineated by site-directed mutagenesis, includes variant residues."
    Tremeau O., Lemaire C., Drevet P., Pinkasfeld S., Ducancel F., Boulain J.-C., Menez A.
    J. Biol. Chem. 270:9362-9369(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 22-83, DISULFIDE BONDS.
  12. "Structure of dimeric and monomeric erabutoxin a refined at 1.5 A resolution."
    Nastopoulos V., Kanellopoulos P.N., Tsernoglou D.
    Acta Crystallogr. D 54:964-974(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 22-83, DISULFIDE BONDS.
  13. "High resolution X-ray analysis of two mutants of a curaremimetic snake toxin."
    Gaucher J.F., Menez R., Arnoux B., Pusset J., Ducruix A.
    Eur. J. Biochem. 267:1323-1329(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 22-83, DISULFIDE BONDS.

Entry informationi

Entry namei3S1EA_LATSE
AccessioniPrimary (citable) accession number: P60775
Secondary accession number(s): P01435
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 6, 2016
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.